The minimum peptide epitope from the influenza virus matrix protein. Extra and intracellular loading of HLA-A2 - PubMed (original) (raw)
. 1991 Dec 15;147(12):4047-53.
Affiliations
- PMID: 1721637
The minimum peptide epitope from the influenza virus matrix protein. Extra and intracellular loading of HLA-A2
M A Bednarek et al. J Immunol. 1991.
Abstract
Influenza virus matrix protein-derived peptides were synthesized based on the amino acid motifs for HLA-A2 bound self peptides. Among these peptides a nonamer (amino acids 58 through 66: G I L G F V F T L) was found to be 100 to 1000 times more effective than the commonly used peptide 57-68 (K G I L G F V F T L T V) in sensitizing HLA-A2+ target cells to lysis by influenza virus specific cytotoxic T lymphocytes. The sensitizing activity of the 12-mer 57-68 was not due to contamination with shorter and more active peptides. Intracellular expression of peptide 58-66 (mediated by a stable expression plasmid with DNA coding for this peptide) also sensitized HLA-A2+ cells to lysis. Peptide 58-66 stimulated human PBMC to generate CTL that recognized peptides 58-66 and 57-68 in association with HLA-A2.
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